ID   DRAA_ECOLX              Reviewed;         160 AA.
AC   P24093;
DT   01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-1992, sequence version 1.
DT   25-MAY-2022, entry version 100.
DE   RecName: Full=Dr hemagglutinin structural subunit;
DE   Flags: Precursor;
GN   Name=draA;
OS   Escherichia coli.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Serotype O75;
RX   PubMed=1670929; DOI=10.1128/iai.59.1.261-268.1991;
RA   Swanson T.S., Bilge S.S., Nowicki B., Moseley S.L.;
RT   "Molecular structure of the Dr adhesin: nucleotide sequence and mapping of
RT   receptor-binding domain by use of fusion constructs.";
RL   Infect. Immun. 59:261-268(1991).
RN   [2]
RP   PROTEIN SEQUENCE OF 22-46.
RC   STRAIN=5026, and 950;
RX   PubMed=1968432; DOI=10.1128/iai.58.3.695-702.1990;
RA   Kist M.L., Salit I.E., Hoffman T.;
RT   "Purification and characterization of the Dr hemagglutinins expressed by
RT   two uropathogenic Escherichia coli strains.";
RL   Infect. Immun. 58:695-702(1990).
CC   -!- FUNCTION: Hemagglutinins of uropathogenic E.coli mediate adherence to
CC       the upper urinary tract. These adhesins bind to the Dr blood group
CC       antigen and also agglutinate human erythrocytes in the presence of D-
CC       mannose (mannose-resistant hemagglutination (MRHA)).
CC   -!- SUBCELLULAR LOCATION: Fimbrium.
CC   -!- SIMILARITY: Belongs to the Dr-adhesin family. {ECO:0000305}.
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DR   EMBL; M62834; AAA23709.1; -; Genomic_DNA.
DR   RefSeq; WP_063269203.1; NZ_NJLI01000067.1.
DR   PDB; 1USQ; X-ray; 1.90 A; A/B/C/D/E/F=21-160.
DR   PDB; 1UT1; X-ray; 1.70 A; A/B/C/D/E/F=21-160.
DR   PDB; 2JKJ; X-ray; 2.30 A; A/B/C/D/E/F=23-160.
DR   PDB; 2JKL; X-ray; 1.90 A; A/B/C/D/E/F=23-160.
DR   PDB; 2JKN; X-ray; 1.90 A; A/B/C/D/E/F=23-160.
DR   PDB; 2W5P; X-ray; 1.90 A; A/B/C=23-160.
DR   PDBsum; 1USQ; -.
DR   PDBsum; 1UT1; -.
DR   PDBsum; 2JKJ; -.
DR   PDBsum; 2JKL; -.
DR   PDBsum; 2JKN; -.
DR   PDBsum; 2W5P; -.
DR   AlphaFoldDB; P24093; -.
DR   BMRB; P24093; -.
DR   SMR; P24093; -.
DR   DrugBank; DB07492; Bromamphenicol.
DR   DrugBank; DB00446; Chloramphenicol.
DR   DrugBank; DB07565; Chloramphenicol succinate.
DR   DrugBank; DB08621; Thiamphenicol.
DR   EvolutionaryTrace; P24093; -.
DR   GO; GO:0009289; C:pilus; IEA:UniProtKB-SubCell.
DR   Gene3D; 2.60.40.1570; -; 1.
DR   InterPro; IPR006713; Adhesin_Dr.
DR   InterPro; IPR021020; Adhesin_Dr_signal_peptide.
DR   InterPro; IPR008966; Adhesion_dom_sf.
DR   InterPro; IPR037028; Dr_adhesin_sf.
DR   Pfam; PF04619; Adhesin_Dr; 1.
DR   Pfam; PF12393; Dr_adhesin; 1.
DR   SUPFAM; SSF49401; SSF49401; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Fimbrium; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000269|PubMed:1968432"
FT   CHAIN           22..160
FT                   /note="Dr hemagglutinin structural subunit"
FT                   /id="PRO_0000000874"
FT   REGION          22..75
FT                   /note="Receptor-binding"
FT                   /evidence="ECO:0000255"
FT   VARIANT         43
FT                   /note="R -> Y (in strain: 950 and 5026)"
FT   STRAND          22..37
FT                   /evidence="ECO:0007829|PDB:1UT1"
FT   STRAND          39..46
FT                   /evidence="ECO:0007829|PDB:1UT1"
FT   STRAND          50..52
FT                   /evidence="ECO:0007829|PDB:1UT1"
FT   HELIX           53..55
FT                   /evidence="ECO:0007829|PDB:1UT1"
FT   STRAND          61..71
FT                   /evidence="ECO:0007829|PDB:1UT1"
FT   STRAND          75..81
FT                   /evidence="ECO:0007829|PDB:1UT1"
FT   HELIX           83..85
FT                   /evidence="ECO:0007829|PDB:1UT1"
FT   STRAND          90..95
FT                   /evidence="ECO:0007829|PDB:1UT1"
FT   STRAND          101..111
FT                   /evidence="ECO:0007829|PDB:1UT1"
FT   STRAND          114..117
FT                   /evidence="ECO:0007829|PDB:1UT1"
FT   STRAND          120..125
FT                   /evidence="ECO:0007829|PDB:1UT1"
FT   STRAND          130..139
FT                   /evidence="ECO:0007829|PDB:1UT1"
FT   STRAND          146..159
FT                   /evidence="ECO:0007829|PDB:1UT1"
SQ   SEQUENCE   160 AA;  17058 MW;  8F282F8FF1500788 CRC64;
     MKKLAIMAAA SMVFAVSSAH AGFTPSGTTG TTKLTVTEEC QVRVGDLTVA KTRGQLTDAA
     PIGPVTVQAL GCDARQVALK ADTDNFEQGK FFLISDNNRD KLYVNIRPTD NSAWTTDNGV
     FYKNDVGSWG GIIGIYVDGQ QTNTPPGNYT LTLTGGYWAK